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Title: RNA-Dependent Cysteine Biosynthesis in Bacteria and Archaea

Journal Article · · mBio
 [1];  [1];  [2];  [3];  [3];  [4]; ; ;
  1. Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA
  2. Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA, Department of Biological Science and Technology, Tokyo University of Science, Katsushika-ku, Tokyo, Japan
  3. Department of Energy Joint Genome Institute (DOE JGI), Walnut Creek, California, USA
  4. Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA, Department of Chemistry, Yale University, New Haven, Connecticut, USA

ABSTRACT The diversity of the genetic code systems used by microbes on earth is yet to be elucidated. It is known that certain methanogenic archaea employ an alternative system for cysteine (Cys) biosynthesis and encoding; tRNACysis first acylated with phosphoserine (Sep) byO-phosphoseryl-tRNA synthetase (SepRS) and then converted to Cys-tRNACysby Sep-tRNA:Cys-tRNA synthase (SepCysS). In this study, we searched all genomic and metagenomic protein sequence data in the Integrated Microbial Genomes (IMG) system and at the NCBI to reveal new clades of SepRS and SepCysS proteins belonging to diverse archaea in the four major groups (DPANN,Euryarchaeota, TACK, and Asgard) and two groups of bacteria (“CandidatusParcubacteria” andChloroflexi). Bacterial SepRS and SepCysS charged bacterial tRNACysspecies with cysteinein vitro. Homologs of SepCysE, a scaffold protein facilitating SepRS-SepCysS complex assembly in Euryarchaeota class I methanogens, are found in a few groups of TACK and Asgard archaea, whereas the C-terminally truncated homologs exist fused or genetically coupled with diverse SepCysS species. Investigation of the selenocysteine (Sec)- and pyrrolysine (Pyl)-utilizing traits in SepRS-utilizing archaea and bacteria revealed that the archaea carrying full-length SepCysE employ Sec and that SepRS is often found in Pyl-utilizing archaea andChloroflexibacteria. We further discuss possible contributions of the SepRS-SepCysS system for sulfur assimilation, methanogenesis, and other metabolic processes requiring large amounts of iron-sulfur enzymes or Pyl-containing enzymes.

Research Organization:
Yale Univ., New Haven, CT (United States); Univ. of California, Los Angeles, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences, and Biosciences Division; Japan Society for the Promotion of Science (JSPS); National Institutes of Health (NIH)
Grant/Contract Number:
FG02-98ER20311; AC02-05CH11231; R01GM22854; R35GM122560
OSTI ID:
1786910
Alternate ID(s):
OSTI ID: 1425739
Journal Information:
mBio, Journal Name: mBio Vol. 8 Journal Issue: 3; ISSN 2161-2129
Publisher:
American Society for MicrobiologyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 19 works
Citation information provided by
Web of Science

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